Criterion cell

Manufactured by Bio-Rad

Sourced in United States

The Criterion Cell is a laboratory equipment designed for electrophoresis applications. It facilitates the separation and analysis of biological macromolecules, such as proteins and nucleic acids, based on their size and charge. The core function of the Criterion Cell is to provide a controlled environment for the electrophoretic process.

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Criterion™ Vertical Electrophoresis Cell (9 citations) Criterion Cell system (7 citations) Mini Trans-Blot Cell and Criterion Blotter (3 citations) Criterion Dodeca Cell (3 citations) Criterion Cell Electrophoresis System (2 citations) Midi Criterion™ Cell (2 citations) Criterion Vertical Electrophoresis Cell and Trans-Blot Turbo Transfer System (2 citations)

36 protocols using criterion cell

Proteomics Analysis of Rubisco Depletion

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One-dimensional gel electrophoresis was used to resolve proteins from the bound and flow-through fractions obtained during Rubisco depletion on the Seppro column. Ten μl of each fraction containing approximately 10 μg of protein was mixed with 10 μl of gel sample buffer (0.2 M Tris-HCl, pH 6.8, 2% SDS, 10% glycerol,0.02% bromophenol blue) and separated on a 1.0 mm, 12.5% Criterion Tris/HCl gel in a Criterion Cell (Bio-Rad) (13.3 cm × 8.7 cm) at a constant voltage of 150 V. The separated proteins were visualized using Bio-Safe Coomassie Blue stain (Bio-Rad).
For phosphoproteome analysis, 200 μl (200 μg) of IMAC-enriched phosphoprotein sample was mixed with 200 μl of rehydration buffer (7 M urea, 2 M thiorea, 2% CHAPS, 10 mM DTT, 0.5% IPG buffer, pH 3–10), resolved by 2-DE and visualized by silver staining ¹⁰. Gel images were recorded using an ImageScanner (GE Healthcare) and Phoretix 2D software (v2004) was used to measure the total number of protein spots visualized in each 2-DE gel image. Proteins of interest were excised manually from each gel and digested with trypsin using a MassPREP protein digestion station, according to the protocol (digestion 5.0) recommended by the manufacturer (Micromass, Manchester, UK). Preparation of tryptic peptide samples for LC-MS/MS analysis was carried out as previously described.[11 (link)]

Aryal U.K., Ross A.R, & Krochko J.E. (2015). Enrichment and Analysis of Intact Phosphoproteins in Arabidopsis Seedlings. PLoS ONE, 10(7), e0130763.

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Two-Dimensional Gel Electrophoresis and Immunoblotting

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IsoElectric focusing (IEF) was performed on IPG 11 cm long (pH 3–10) strips (Biorad) using 200 μg of proteins. IEF was carried out using a PROTEAN IEF Cell (Biorad) as follows: passive rehydration (10 h), active rehydration at 50 V (12 h), and migration (250 V for 15 min, 8000 V for 2h30, and a final phase of 8000 V up to a maximum of 35,000 V/h). Following IEF, the focused strips were rotated in 135 mM dithiothreitol (Euromedex) in equilibration buffer (6 M urea; 2% SDS; 0.375 M Tris–HCl pH 8.8; 20% glycerol, 10 mL for 15 min) and, subsequently, in 135 mM iodoacetamide (Sigma) in equilibration buffer (10 mL for 15 min). Second-dimension gels (1 mm thick, 4–15% gradient acrylamide, Criterion TGX—IPG 11cm+1well precast gels, Biorad) were run (5 h, 80 V) using the criterion cell (Biorad). Proteins were then transferred on activated PVDF membranes and blocked with TBS-T, 5% w/v BSA. Membranes were hybridized with pre-immune or immune serum (1:1000, overnight, 4 °C), anti-beta-actin (1:2500, Sigma), or anti-GAPDH (1:10,000, Sigma) and secondary antibodies were applied after three washing steps in TBS-T: rabbit HRP-conjugated anti-ATS IgG antibody (1:1000, 1 h, RT) or HRP-conjugated anti-rabbit IgG antibody (BI 2407, 1:1000 for beta-actin and 1:5000 for GAPDH, Abliance). Protein spots were finally revealed by ECL as described above.

Chorfa A., Goubely C., Henry-Berger J., Guiton R., Drevet J.R, & Saez F. (2021). Identification of Arvicola terrestris scherman Sperm Antigens for Immune Contraceptive Purposes. International Journal of Molecular Sciences, 22(18), 9965.

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SNP Detection in Dutch Saanen Bucks

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For detection of SNPs on Dutch Saanen bucks, restricted representation libraries (RRL) were constructed as described by Kraus et al [19] (link). In short, equal amounts of DNA from the 17 bucks were combined into two pools each consisting of 25 µg of DNA. Aliquots of 5 µg for each pool were digested with either AluI or HhaI (10 units per reaction, Pharmacia). The digested pools in Orange loading dye (Fermentas) were size-fractionated on precast 10% polyacrylamide in 1xTBE with the Criterion™ Cell (BioRad). After staining, the target fragment size range of 110–130 bp was sliced out of the gel. The gel slice was sheared by nesting a 0.5ml eppendorf tube (with a hole in the bottom formed with a needle) containing the gel slice inside a 2ml eppendorf tube, and centrifuged at 14000 rpm for 2 minutes. The sheared gel pieces were covered with 300ul DNA recovery buffer (8mM Tris pH 8.0, 0.08mM EDTA, 1.25M ammonium acetate), vortexed, and eluted at 4°C overnight, followed by 15 minutes incubation at 65°C. The DNA was recovered using the Montage DNA gel extraction devices (Millipore) and resuspended in DNA hydration solution (Gentra Systems).

Tosser-Klopp G., Bardou P., Bouchez O., Cabau C., Crooijmans R., Dong Y., Donnadieu-Tonon C., Eggen A., Heuven H.C., Jamli S., Jiken A.J., Klopp C., Lawley C.T., McEwan J., Martin P., Moreno C.R., Mulsant P., Nabihoudine I., Pailhoux E., Palhière I., Rupp R., Sarry J., Sayre B.L., Tircazes A., Jun W.a.n.g., Wang W, & Zhang W. (2014). Design and Characterization of a 52K SNP Chip for Goats. PLoS ONE, 9(1), e86227.

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SDS-PAGE Analysis of Mustard Seed Proteins

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Mustard seed extracts normalized to equal amounts of protein (10 µg) were subjected to SDS-PAGE under reducing and non-reducing conditions using pre-cast Any KD TGX gels (Bio-Rad Laboratories, Hercules, CA, USA) according to Laemmli [26 (link)]. The soluble extracts were mixed with an equal volume of Laemmli sample buffer with 5% (v/v) of β-mercaptoethanol (β-ME) and boiled for 5 min. Alternatively, electrophoresis was performed under non-reducing conditions by omitting the addition of β-ME. The gels were run at a constant voltage of 150 V for 90 min using TGS buffer (25 mM Tris, 192 mM glycine, and 0.1% SDS) in a Criterion cell (Bio-Rad). A molecular weight standard (Precision Plus Protein Standard) was included on each gel. After electrophoresis, gels were stained with Coomassie Brilliant Blue. Images were acquired by scanning stained gels using an Image Scanner III (GE Healthcare, Salt Lake City, UT, USA) operated by LabScan 6.0 software (GE Healtcare). For image and densitometry analysis, the Image Quant TL 7.0 Software (GE Healtcare) was used.

L’Hocine L., Pitre M, & Achouri A. (2019). Detection and Identification of Allergens from Canadian Mustard Varieties of Sinapis alba and Brassica juncea. Biomolecules, 9(9), 489.

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SDS-PAGE and Western Blot Protocol

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SDS-PAGE was carried out using Criterion^™ TGX^™ precast 4–15% gradient 18-well midi gels (Bio-Rad, 5671084). Samples were prepared in 4X Laemmli sample buffer (Bio-Rad, 1610747) and 10% β-mercapto ethanol (Acros organics, 149582500). Gels were run in Criterion^™ cell (Bio-Rad, 1656001) using PowerPac^™ power supply (Bio-Rad, 1645050), SDS running buffer (Tris base: 0.2501 M, Glycine: 1.924 M, SDS: 0.03467 M) for 70 minutes at 150 constant volts. Transfer to membranes was carried out in a Criterion^™ Blotter (Bio-Rad, 1704071), transfer buffer (Tris base: 25 mM, Glycine: 192 mM, Methanol: 20% v/v) over 1 hour at 100 constant volts for samples of DAOY Tau-GFP, or 3 hours at 350 constant mA for mHTT MEF. All transfers were carried out at 4°C onto 0.45 μM nitrocellulose membranes (Bio-Rad, 1620167). Membranes were incubated with antibodies overnight at 4°C, washed three times and incubated with secondary Hrp-conjugated antibodies at room temperature for 1 hour. Membranes were then exposed to ECL (Amersham Cytiva, RPN2106) or ECL prime (Amersham Cytiva, RPN2236) prior to imaging using a ChemiDoc^™ touch gel imaging system (Bio-Rad, 1708370). Protein size ladders used were either precision plus protein dual color (Bio-Rad, 161–0374) or Himark pre-stained HMW protein standard (ThermoFisher, LC5699). All images were quantified using Image Lab software (Bio-Rad, version 6.0.1).

Benyair R., Giridharan S.S., Rivero-Ríos P., Hasegawa J., Bristow E., Eskelinen E.L., Shmueli M.D., Fishbain-Yoskovitz V., Merbl Y., Sharkey L.M., Paulson H.L., Hanson P.I., Patnaik S., Al-Ramahi I., Botas J., Marugan J, & Weisman L.S. (2023). Upregulation of the ESCRT pathway and multivesicular bodies accelerates degradation of proteins associated with neurodegeneration. Autophagy reports, 2(1), 2166722.

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Northern Blot Analysis of EBV, GFP, and GAPDH

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Total mRNA was purified from cell pellets using the Dynabeads mRNA DIRECT Purification kit (Thermo Fisher Scientific) according to the manufacturer’s instructions. RNA was denatured at 70°C for 5 minutes in 1x RNA loading dye (Thermo Fisher Scientific) and resolved on a 1.5% agarose gel using a Mini-Protean Tetra Cell system (Bio-Rad) in 1x TBE buffer (Invitrogen). After electrophoresis, the RNA was transferred onto a BrightStar Plus positively charged Nylon membrane (Invitrogen) using a Criterion cell (Bio-Rad) in 0.5 x TBE buffer and UV-crosslinked to the membrane at 300 mJ/cm². The membrane was hybridized with biotinylated probes purchased from IDT, recognizing the EBV transactivator transcripts (5′-CATAAGCTTGATAAGCATTCTCAGGAGCAGGCTGAGGGGC-3′), GFP (5′- TCGGCGCGGGTCTTGTAGTTGCCGTCGTCCTTGAAGAAGA-3′), or GAPDH (5′-TGGTGCAGGAGGCATTGCTGATGATCTTGAGGCTGTTG-3′), in ULTRAhyb-Oligo Hybridization Buffer (Invitrogen) at 42°C overnight, followed by incubation with a streptavidin-alkaline phosphatase conjugate for detection (Invitrogen). Imaging was performed using CDP-Star luminescent substrate (Life Technologies), and bands were detected using a LAS Imagequant 4000 luminescent imaging system (GE Life Sciences).

van Gent M., Reich A., Velu S.E, & Gack M.U. (2021). Nonsense-mediated decay controls the reactivation of the oncogenic herpesviruses EBV and KSHV. PLoS Biology, 19(2), e3001097.

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Quantification of eNOS Protein Levels

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Lung tissue was lysed (RIPA buffer; 50 mM Tris-HCl, pH 8.0, with 150 mM sodium chloride, 1.0% Igepal CA-630 (NP-40), 0.5% sodium deoxycholate, and 0.1% sodium dodecyl sulfate) and protein concentration was measured with bicinchoninic assay (BCA, Sigma-Aldrich, St. Louis, MO, USA). Equal amounts of total protein (20 µg) were separated by SDS-PAGE on a Bio-Rad Criterion cell using Criterion precast gels (Bio-Rad, Hercules, CA, USA). Proteins were electroblotted onto polyvinylidene fluoride (PVDF) membranes. Membranes were blocked with 5% bovine serum albumin (BSA) (Sigma-Aldrich) and incubated with an antibody against eNOS (1:300, ABCAm, Cambridge, UK) in 1% BSA overnight at 4℃. After incubation with the secondary, peroxidase-coupled antibody (Polyclonal Rabbit Anti-Mouse Ig/HRP P0260; DakoCytomation, Carpinteria, CA, USA) detection was accomplished by using enhanced chemiluminescence solution (Western Lightning reagent; Perkin Elmer, Boston, MA, USA) and a ChemiDoc XRS chemiluminescence detection system (Bio-Rad). Densitometric eNOS quantification was accomplished using NIH ImageJ software (1.47, Bethesda, MD, USA). Results were normalized to the respective GAPDH bands.

Schreiber C., Eilenberg M.S., Panzenboeck A., Winter M.P., Bergmeister H., Herzog R., Mascherbauer J., Lang I.M, & Bonderman D. (2017). Combined oral administration of L-arginine and tetrahydrobiopterin in a rat model of pulmonary arterial hypertension. Pulmonary Circulation, 7(1), 89-97.

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Aspergillus oryzae Protoplast Transformation

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Example 5

Aspergillus oryzae JaL355 (WO 2002/40694) protoplasts were prepared according to the method of Christensen et al., 1988, Bio/Technology 6: 1419-1422, which were transformed with approximately 2 μg of pSMai207. The transformation yielded about 30 transformants. Ten transformants were isolated to individual Minimal Medium plates.

Confluent Minimal Medium plates of each of the transformants were washed with 5 ml of 0.01% TWEEN® 20 and inoculated separately into 25 ml of M410 medium in 125 ml glass shake flasks and incubated at 34° C., 250 rpm. After 5 days incubation, 5 μl of supernatant from each culture were analyzed on CRITERION® Tris-HCl gels (Bio-Rad Laboratories, Hercules, Calif., USA) with a CRITERION® Cell (Bio-Rad Laboratories, Hercules, Calif., USA), according to the manufacturer's instructions. The resulting gels were stained with BIO-SAFE™ Coomassie Stain (Bio-Rad Laboratories, Hercules, Calif., USA). SDS-PAGE profiles of the cultures showed that the majority of the transformants had an expected 24 KDa band size. A confluent plate of transformant 3 was washed with 10 ml of 0.01% TWEEN® 80 and inoculated into a 2 liter Fernbach containing 500 ml of M410 medium to generate broth for characterization of the enzyme. The culture was harvested on day 5 and filtered using a 0.22 μm EXPRESS™ PLUS Membrane (Millipore, Billerica, Mass., USA).

US10006012B2. Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same (2018-06-26). Novozymes, Inc. [US]. Inventors: Suchindra Maiyuran [US], Randall Kramer [US], Paul Harris [US].

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Deglycosylation and Dephosphorylation of Whole Cell Lysates

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Whole cell lysates were extracted from HCT116 cells treated with Nutlin-3a or DMSO using RIPA buffer (Thermo Fisher Scientific) without protease or phosphatase inhibitors. Lysates were exposed to PNGase F and Shrimp Alkaline Phosphatase (New England Biolabs) enzymes. Samples were preincubated with 1× Glycoprotein denaturing buffer (New England Biolabs) for 10 min at 100°C. Next, 1× GlycoBuffer, 1% NP-40 and 1× Cut Smart Buffer (New England Biolabs) were added to the lysate and incubated for 1 h at 37°C. 10 μg of whole cell lysates were incubated for 1 h at 37°C as control. 4× LDS buffer was added to all samples to a final concentration of 1×. All samples were boiled at 100°C for 5 min. Finally, proteins were separated using a precast 3–8% Criterion Tris-Acetate protein gel (Bio Rad) and a Criterion Cell (Bio Rad) in Tris-acetate buffer.

Coronel L., Riege K., Schwab K., Förste S., Häckes D., Semerau L., Bernhart S.H., Siebert R., Hoffmann S, & Fischer M. (2021). Transcription factor RFX7 governs a tumor suppressor network in response to p53 and stress. Nucleic Acids Research, 49(13), 7437-7456.

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Isoelectric Focusing of Cytochrome c4

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Isoelectric focusing (IEF) of the purified cyt c₄ was carried out with Criterion IEF Gel pH3–10 (Bio-Rad) using a Bio-Rad Criterion™ cell. The samples in a 10 mM Tris buffer at pH 7.5 were mixed with equal volume of sample buffer (50% glycerol). IEF Standards 4.45–9.6 (Bio-Rad) were employed for calibration of pI values. The gel was run at constant voltage in three steps (100 V for 60 min, 250 V for 60 min and 500 V for 30 min) and stained using Coomassie G-250 (Bio-Rad).

Carpenter J.M., Zhong F., Ragusa M.J., Louro R.O., Hogan D.A, & Pletneva E.V. (2019). Structure and Redox Properties of the Diheme Electron Carrier Cytochrome c4 from Pseudomonas aeruginosa. Journal of inorganic biochemistry, 203, 110889.

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